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Protein Short-Time Diffusion in a Naturally Crowded Environment

Grimaldo, Marco; Lopez, Hender; Beck, Christian; Roosen-Runge, Felix LU ; Moulin, Martine; Devos, Juliette M.; Laux, Valerie; Härtlein, Michael; Da Vela, Stefano and Schweins, Ralf, et al. (2019) In Journal of Physical Chemistry Letters 10(8). p.1709-1715
Abstract


The interior of living cells is a dense and polydisperse suspension of macromolecules. Such a complex system challenges an understanding in terms of colloidal suspensions. As a fundamental test we employ neutron spectroscopy to measure the diffusion of tracer proteins (immunoglobulins) in a cell-like environment (cell lysate) with explicit control over crowding conditions. In combination with Stokesian dynamics simulation, we address protein diffusion on nanosecond time scales where hydrodynamic interactions dominate over negligible protein collisions. We successfully link the experimental results on these complex, flexible molecules with coarse-grained simulations providing... (More)


The interior of living cells is a dense and polydisperse suspension of macromolecules. Such a complex system challenges an understanding in terms of colloidal suspensions. As a fundamental test we employ neutron spectroscopy to measure the diffusion of tracer proteins (immunoglobulins) in a cell-like environment (cell lysate) with explicit control over crowding conditions. In combination with Stokesian dynamics simulation, we address protein diffusion on nanosecond time scales where hydrodynamic interactions dominate over negligible protein collisions. We successfully link the experimental results on these complex, flexible molecules with coarse-grained simulations providing a consistent understanding by colloid theories. Both experiments and simulations show that tracers in polydisperse solutions close to the effective particle radius R
eff
= R
i

3

1/3
diffuse approximately as if the suspension was monodisperse. The simulations further show that macromolecules of sizes R > R
eff
(R < R
eff
) are slowed more (less) effectively even at nanosecond time scales, which is highly relevant for a quantitative understanding of cellular processes.

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organization
publishing date
type
Contribution to journal
publication status
published
subject
in
Journal of Physical Chemistry Letters
volume
10
issue
8
pages
7 pages
publisher
The American Chemical Society (ACS)
external identifiers
  • scopus:85064159263
ISSN
1948-7185
DOI
10.1021/acs.jpclett.9b00345
language
English
LU publication?
yes
id
d3ee8428-8a92-492e-b877-ec4f272765b5
date added to LUP
2019-05-09 11:28:10
date last changed
2019-05-14 04:59:34
@article{d3ee8428-8a92-492e-b877-ec4f272765b5,
  abstract     = {<p><br>
                                                         The interior of living cells is a dense and polydisperse suspension of macromolecules. Such a complex system challenges an understanding in terms of colloidal suspensions. As a fundamental test we employ neutron spectroscopy to measure the diffusion of tracer proteins (immunoglobulins) in a cell-like environment (cell lysate) with explicit control over crowding conditions. In combination with Stokesian dynamics simulation, we address protein diffusion on nanosecond time scales where hydrodynamic interactions dominate over negligible protein collisions. We successfully link the experimental results on these complex, flexible molecules with coarse-grained simulations providing a consistent understanding by colloid theories. Both experiments and simulations show that tracers in polydisperse solutions close to the effective particle radius R                             <br>
                            <sub>eff</sub><br>
                                                          = R                             <br>
                            <sub>i</sub><br>
                                                         <br>
                            <sup>3</sup><br>
                                                         <br>
                            <sup>1/3</sup><br>
                                                          diffuse approximately as if the suspension was monodisperse. The simulations further show that macromolecules of sizes R &gt; R                             <br>
                            <sub>eff</sub><br>
                                                          (R &lt; R                             <br>
                            <sub>eff</sub><br>
                                                         ) are slowed more (less) effectively even at nanosecond time scales, which is highly relevant for a quantitative understanding of cellular processes.                         <br>
                        </p>},
  author       = {Grimaldo, Marco and Lopez, Hender and Beck, Christian and Roosen-Runge, Felix and Moulin, Martine and Devos, Juliette M. and Laux, Valerie and Härtlein, Michael and Da Vela, Stefano and Schweins, Ralf and Mariani, Alessandro and Zhang, Fajun and Barrat, Jean Louis and Oettel, Martin and Forsyth, V. Trevor and Seydel, Tilo and Schreiber, Frank},
  issn         = {1948-7185},
  language     = {eng},
  month        = {04},
  number       = {8},
  pages        = {1709--1715},
  publisher    = {The American Chemical Society (ACS)},
  series       = {Journal of Physical Chemistry Letters},
  title        = {Protein Short-Time Diffusion in a Naturally Crowded Environment},
  url          = {http://dx.doi.org/10.1021/acs.jpclett.9b00345},
  volume       = {10},
  year         = {2019},
}